TDRD3 (Tudor domain-containing protein 3) is a multifunctional protein involved in RNA metabolism, transcriptional regulation, and epigenetic processes. It contains a Tudor domain, which recognizes methylated arginine residues, enabling interactions with proteins like arginine-methylated histones or RNA-binding proteins. TDRD3 plays roles in DNA damage repair, mRNA splicing, and gene silencing, and it is implicated in cancer progression and neurological disorders.
TDRD3 antibodies are essential tools for studying its expression, localization, and molecular interactions. These antibodies are typically developed in rabbits or mice using immunogenic peptide sequences derived from conserved regions of the TDRD3 protein. Validated through techniques like Western blotting, immunoprecipitation, and immunofluorescence, they help identify TDRD3 in various tissues and cell types.
Research using TDRD3 antibodies has revealed its association with transcriptional coactivation (e.g., binding steroid receptors) and participation in DNA repair pathways (e.g., interacting with TOP3B). Dysregulation of TDRD3 is linked to cancers, such as breast and prostate cancer, and neurodevelopmental conditions. Commercial TDRD3 antibodies often undergo specificity testing via knockout cell lines to minimize cross-reactivity. Their applications span basic research, biomarker studies, and therapeutic target validation.